Zobrazeno 1 - 10
of 29
pro vyhledávání: '"S K, Chapman"'
Autor:
S. Daff, M. A. Noble, D. H. Craig, S. L. Rivers, S. K. Chapman, A. W. Munro, S. Fujiwara, E. Rozhkova, I. Sagami, T. Shimizu
Publikováno v:
Biochemical Society Transactions. 29:147-152
The nitric oxide synthases (NOSs) are dimeric flavocytochromes consisting of an oxygenase domain with cytochrome P450-like Cys-ligated haem, coupled to a diflavin reductase domain, which is related to cytochrome P450 reductase. The NOSs catalyse the
Autor:
Robert P. Hanzlik, K. L. Turner, M. A. Noble, Luca Quaroni, S. K. Chapman, Andrew W. Munro, George D. Chumanov
Publikováno v:
Biochemistry. 37:15799-15807
omega-Imidazolyl carboxylic acids (C10-C12) have been used as probes of the active site and catalytic mechanism of the fatty acid hydroxylase P-450 BM3 from Bacillus megaterium. These compounds are the most potent inhibitors of P-450 BM3 yet reported
Publikováno v:
Biochemistry. 35:6345-6350
Flavocytochrome b2 from Saccharomyces cerevisiae couples L-lactate dehydrogenation to cytochrome c reduction in the mitochondrial intermembrane space. The catalytic cycle for this process can be described in terms of five consecutive electron-transfe
Autor:
Forbes D C Manson, C Bell, P White, Simon Daff, Sharp Re, Duncan M. Short, S K Chapman, G A Reid
Publikováno v:
Biochemistry. 35:6351-6357
Flavocytochrome b2 from Saccharomyces cerevisiae couples L-lactate dehydrogenation to cytochrome c reduction. At 25 degrees C, 0.10 M ionic strength, and saturating L-lactate concentration, the turnover rate is 207 s-1 [per cytochrome c reduced; Mile
Publikováno v:
ChemInform. 22
Publikováno v:
Biochemistry. 41(13)
Flavocytochrome b(2) catalyzes the oxidation of L-lactate to pyruvate and the transfer of electrons to cytochrome c. The enzyme consists of a flavin-binding domain, which includes the active site for lacate oxidation, and a b(2)-cytochrome domain, re
Publikováno v:
The Biochemical journal. 359(Pt 2)
The side chain of residue Arg(238) in morphinone reductase (MR) is located close to the N-1/C-2 carbonyl region of the flavin isoalloxazine ring. During enzyme reduction negative charge develops in this region of the flavin. The positioning of a posi
Autor:
A W, Munro, M A, Noble, T W, Ost, A J, Green, K J, McLean, L, Robledo, C S, Miles, J, Murdoch, S K, Chapman
Publikováno v:
Sub-cellular biochemistry. 35
Autor:
C G, Mowat, S K, Chapman
Publikováno v:
Sub-cellular biochemistry. 35
Publikováno v:
The Biochemical journal. 349(Pt 1)
Shewanella frigidimarina NCIMB400 is a non-fermenting, facultative anaerobe from the gamma group of proteobacteria. When grown anaerobically this organism produces a wide variety of periplasmic c-type cytochromes, mostly of unknown function. We have